The Eukaryote Linear Motif resource for Functional Sites in Proteins
Accession:
Functional site class:
MYND domain binding motif.
Functional site description:
The MYND domain is a zinc binding domain that is involved in protein-protein interactions mainly in the context of transcriptional regulation. It is named after Myeloid, Nervy, and DEAF-1, which are the three most characterized proteins that contain the MYND domain. Only a small number of MYND domain containing proteins have been identified and they are involved in various biological processes such as cell proliferation, apoptosis, adhesion, migration, and tumorigenesis and oxygen homeostasis. MYND domain typically binds a proline-rich motif in their interacting partners, however they have different binding specificities.
ELMs with same func. site: LIG_MYND_1  LIG_MYND_2  LIG_MYND_3 
ELM Description:
The PxLxP motif is recognized by a subset of MYND domain containing proteins. The target specificity is mainly due to the highly charged surface of the MYND domain with a positive face consisting of C-terminal residues on one side, and a negatively charged region on the other side. The positive charge of these side chains could mediate long-range electrostatic interactions with the negative charges that may flank the PxLxP motif. So the interaction might require a longer region, while the PxLxP motif constitutes the core motif.
Pattern: P.L.P
Pattern Probability: 0.0006499
Present in taxon: Metazoa
Interaction Domain:
zf-MYND (PF01753) MYND finger (Stochiometry: 1 : 1)
o See 6 Instances for LIG_MYND_1
o Abstract
The MYND domain is a cysteine-rich structure present in proteins generally implicated in gene regulation and associated with cancers. Some of the MYND domain containing proteins are BS69, Nervy (a transcriptional corepressor), the chimeric fusion protein of acute myelogenous leukemia (AML) and ETO (a nuclear protein that interacts with corepressor molecules), the bone morphogenesis protein receptor-associated molecule1 (BRAM1), SET and MYND domain-containing proteins (SMYD), RACK7, PDCD2, deformed epidermal auto regulatory factor-1 (DEAF-1). The structures of the MYND domain in these proteins demonstrate a tandem zinc-binding motif organized in cross-brace topology (Kateb,2013).
A variant of MYND domain is also found to exist in prolyl hydroxylase domain protein 2 (PHD2) that catalyzes proline hydroxylation of HIFα subunits. Prolyl hydroxylation is an ancient mechanism to transduce changes in oxygen concentration to changes in cellular function. Among the three PHD isoforms, PHD2 is a distinct one as it is predicted to have a MYND-type zinc finger at its N-terminal. It is also the one that is most closely related to the single ancestral PHD and has the capacity to hydroxylate HIF-1α, which is connected to HSP90 pathway (Huang,2002). Depending upon the variations in amino acid sequence of MYND domain, there exist different binding specificities for MYND domain containing proteins and it acts as a scaffold for different cellular and viral protein-protein interactions.
MYND domains usually recognize proline-rich motifs in their partners. The MYND domain of BS69 has been shown to bind viral tumour antigens E1A and EBNA2 as well as with cellular partners such as MGA through a PxLxP motif (Ansieau,2002). The MYND domain of BS69 contains a set of positively charged residues at its C-terminus, which is crucial for interaction with PxLxP ligands. Other MYND domain containing proteins such as RACK7, ETO and DEAF-1, which lack these charged residues fail to interact with the PxLxP motif. The co-repressor-binding MYND domain-containing proteins such as DEAF-1 and ETO have higher degree of sequence similarity and similar binding mode. They can bind to another proline-rich motif PPPLI (Liu,2007). The MYND-type Zinc Finger of PHD2 binds a PxLE motif, which is so far found to exist in HSP90 co-chaperones p23 and FKBP38 (Song,2013).
o 6 selected references:

o 5 GO-Terms:

o 6 Instances for LIG_MYND_1
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Protein NameGene NameStartEndSubsequenceLogic#Ev.OrganismNotes
NACAM_MOUSE Naca 1950 1954 PAEEDELPPLIPPEAVSGGE TP 4 Mus musculus (House mouse)
1 
MGAP_HUMAN MGA 2973 2977 GQSLKVMPCLAPIAAKVGSV TP 4 Homo sapiens (Human)
1 
MGAP_HUMAN MGA 2948 2952 DTLWRPMPKLAPLGLKVANP TP 4 Homo sapiens (Human)
1 
EBNA2_EBVB9 EBNA2 437 441 SHNSPEAPILFPDDWYPPSI TP 5 Human herpesvirus 4 (strain B95-8) (Epstein-Barr virus (strain B95-8))
1 
EBNA2_EBVB9 EBNA2 383 387 NTSSPSMPELSPVLGLHQGQ TP 5 Human herpesvirus 4 (strain B95-8) (Epstein-Barr virus (strain B95-8))
1 
E1A_ADE05 Early E1A 32 113 117 ALGPVSMPNLVPEVIDLTCH TP 4 Human adenovirus 5
1 
Please cite: The Eukaryotic Linear Motif Resource ELM: 10 Years and Counting (PMID:24214962)

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